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Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling

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Bibliographic Details
Main Author: Stone, Shane Ramsay
Other Authors: Jackson, Graham Ellis
Format: Thesis
Language:English
Published: Department of Chemistry 2014
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access_status_str Open Access
author Stone, Shane Ramsay
author2 Jackson, Graham Ellis
author_browse Jackson, Graham Ellis
Stone, Shane Ramsay
author_facet Jackson, Graham Ellis
Stone, Shane Ramsay
author_sort Stone, Shane Ramsay
collection Thesis
description Word processed copy.
format Thesis
id oai:open.uct.ac.za:11427/6289
institution University of Cape Town (South Africa)
language eng
license_str Not specified — see source repository
provenance_str_mv Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository
publishDate 2014
publishDateRange 2014
publishDateSort 2014
publisher Department of Chemistry
publisherStr Department of Chemistry
record_format dspace
source_str UCTD — University of Cape Town Open Access Repository
spelling oai:open.uct.ac.za:11427/6289 Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling Stone, Shane Ramsay Jackson, Graham Ellis Chemistry Word processed copy. Includes bibliographical references. The solution studies aimed to determine the conformations of a series of DMSO solubilised gastrin peptides, G-4, [ß-Ala ¹] G-5 and G-17, so as to establish how the configurations of the biologically relevant sequence were related to each other, and to resolve whether they adopted preferred and conserved conformations in solution. Interproton distance restraints were calculated from measured NOe crosspeak intensities for each peptide. 2014-08-13T14:25:47Z 2014-08-13T14:25:47Z 2006 Doctoral Thesis Doctoral PhD http://hdl.handle.net/11427/6289 eng application/pdf Department of Chemistry Faculty of Science University of Cape Town
spellingShingle Chemistry
Stone, Shane Ramsay
Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling
thesis_degree_str Doctoral
title Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling
title_full Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling
title_fullStr Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling
title_full_unstemmed Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling
title_short Structural characterisation of the solution and membrane-associated conformations of human little gastrin and its bioactive fragments by NMR spectroscopy and molecular modelling
title_sort structural characterisation of the solution and membrane associated conformations of human little gastrin and its bioactive fragments by nmr spectroscopy and molecular modelling
topic Chemistry
url http://hdl.handle.net/11427/6289
work_keys_str_mv AT stoneshaneramsay structuralcharacterisationofthesolutionandmembraneassociatedconformationsofhumanlittlegastrinanditsbioactivefragmentsbynmrspectroscopyandmolecularmodelling